Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (P0AB91)

Identification
Name:Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
Synonyms:
  • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
  • DAHP synthase
  • Phospho-2-keto-3-deoxyheptonate aldolase
Gene Name:aroG
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D- arabino-heptulosonate-7-phosphate (DAHP)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Metabolic pathways eco01100
  • Phenylalanine, tyrosine and tryptophan biosynthesis ec00400
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0Water + 1.0Phosphoenolpyruvic acid ↔ 1.02-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0Water + 1.0Phosphoenolpyruvic acid → 1.0Phosphate + 1.03-deoxy-D-arabino-heptulosonate-7-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0Water + 1.0Phosphoenolpyruvic acid ↔ 1.02-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + 1.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200392-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphateMetaboCard
ECMDB241823-deoxy-D-arabino-heptulosonate-7-phosphateMetaboCard
ECMDB02649D-Erythrose 4-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
3-deoxy-7-phosphoheptulonate synthase activity
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
aromatic amino acid family biosynthetic process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b0754
Gene OrientationClockwise
Centisome Percentage:16.92
Left Sequence End784856
Right Sequence End785908
Gene Sequence:
>1053 bp
ATGAATTATCAGAACGACGATTTACGCATCAAAGAAATCAAAGAGTTACTTCCTCCTGTC
GCATTGCTGGAAAAATTCCCCGCTACTGAAAATGCCGCGAATACGGTTGCCCATGCCCGA
AAAGCGATCCATAAGATCCTGAAAGGTAATGATGATCGCCTGTTGGTTGTGATTGGCCCA
TGCTCAATTCATGATCCTGTCGCGGCAAAAGAGTATGCCACTCGCTTGCTGGCGCTGCGT
GAAGAGCTGAAAGATGAGCTGGAAATCGTAATGCGCGTCTATTTTGAAAAGCCGCGTACC
ACGGTGGGCTGGAAAGGGCTGATTAACGATCCGCATATGGATAATAGCTTCCAGATCAAC
GACGGTCTGCGTATAGCCCGTAAATTGCTGCTTGATATTAACGACAGCGGTCTGCCAGCG
GCAGGTGAGTTTCTCGATATGATCACCCCACAATATCTCGCTGACCTGATGAGCTGGGGC
GCAATTGGCGCACGTACCACCGAATCGCAGGTGCACCGCGAACTGGCATCAGGGCTTTCT
TGTCCGGTCGGCTTCAAAAATGGCACCGACGGTACGATTAAAGTGGCTATCGATGCCATT
AATGCCGCCGGTGCGCCGCACTGCTTCCTGTCCGTAACGAAATGGGGGCATTCGGCGATT
GTGAATACCAGCGGTAACGGCGATTGCCATATCATTCTGCGCGGCGGTAAAGAGCCTAAC
TACAGCGCGAAGCACGTTGCTGAAGTGAAAGAAGGGCTGAACAAAGCAGGCCTGCCAGCA
CAGGTGATGATCGATTTCAGCCATGCTAACTCGTCCAAACAATTCAAAAAGCAGATGGAT
GTTTGTGCTGACGTTTGCCAGCAGATTGCCGGTGGCGAAAAGGCCATTATTGGCGTGATG
GTGGAAAGCCATCTGGTGGAAGGCAATCAGAGCCTCGAGAGCGGGGAGCCGCTGGCCTAC
GGTAAGAGCATCACCGATGCCTGCATCGGCTGGGAAGATACCGATGCTCTGTTACGTCAA
CTGGCGAATGCAGTAAAAGCGCGTCGCGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:350
Protein Molecular Weight:38009
Protein Theoretical pI:7
PDB File:1QR7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
MNYQNDDLRIKEIKELLPPVALLEKFPATENAANTVAHARKAIHKILKGNDDRLLVVIGP
CSIHDPVAAKEYATRLLALREELKDELEIVMRVYFEKPRTTVGWKGLINDPHMDNSFQIN
DGLRIARKLLLDINDSGLPAAGEFLDMITPQYLADLMSWGAIGARTTESQVHRELASGLS
CPVGFKNGTDGTIKVAIDAINAAGAPHCFLSVTKWGHSAIVNTSGNGDCHIILRGGKEPN
YSAKHVAEVKEGLNKAGLPAQVMIDFSHANSSKQFKKQMDVCADVCQQIAGGEKAIIGVM
VESHLVEGNQSLESGEPLAYGKSITDACIGWEDTDALLRQLANAVKARRG
References
External Links:
ResourceLink
Uniprot ID:P0AB91
Uniprot Name:AROG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651339
PDB ID:1QR7
Ecogene ID:EG10079
Ecocyc:EG10079
ColiBase:b0754
Kegg Gene:b0754
EchoBASE ID:EB0077
CCDB:AROG_ECOLI
BacMap:16128722
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Davies, W. D., Davidson, B. E. (1982). "The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12." Nucleic Acids Res 10:4045-4058. Pubmed: 6125934
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Shumilin, I. A., Kretsinger, R. H., Bauerle, R. H. (1999). "Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli." Structure 7:865-875. Pubmed: 10425687
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842